| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000197715 |
| Family | AA3 |
| Protein Properties | Length: 463 Molecular Weight: 51210.5 Isoelectric Point: 6.9185 |
| Chromosome | Chromosome/Scaffold: 01414687 Start: 14181 End: 16199 |
| Description | Long-chain fatty alcohol dehydrogenase family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA3 | 63 | 461 | 2.8e-25 |
| GLQVIYNSTKNIYNIKRDVVVVGSGCGGCVVAVVLASSGHKVIVLEKGNYFTHLDYSSLEAPSHDQLYEAGGIIVTADGKIILQVRSTDNKIKFCWGREY LSAMDTVCERIGVTENCIEEGFQNQVLRKGCENLGFEVDIVPRNSSEKHYCGSCGYGCKKGEKKGTDSTWLVDAVDHGAVILTGCKAEKFVLETGKSESK RKKKCLEVMAKALSNIITKRLQIEAKVTVSACGALLTPHLMLSSGLKNKNIGRNLHLHPVLMAWGYFPDLNLEFKGKNYEDGIITSVHKVVSADSKAKAI IETPTLGLGTFSALCPWEFGEDIKNRMLKFSRTVHLISIIRDWGSRVVTKGGRDFFDMVTADERPQSLVENWTTYSSAHQMRSCRMGIKAKEGVVDENG | |||
| Full Sequence |
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| Protein Sequence Length: 463 Download |
| MEVNENAENS IWQAIGYHVE SDDQGDLKNP SKVQEQERPL QNGIIETMLE TDTTLLNSLE 60 QKGLQVIYNS TKNIYNIKRD VVVVGSGCGG CVVAVVLASS GHKVIVLEKG NYFTHLDYSS 120 LEAPSHDQLY EAGGIIVTAD GKIILQVRST DNKIKFCWGR EYLSAMDTVC ERIGVTENCI 180 EEGFQNQVLR KGCENLGFEV DIVPRNSSEK HYCGSCGYGC KKGEKKGTDS TWLVDAVDHG 240 AVILTGCKAE KFVLETGKSE SKRKKKCLEV MAKALSNIIT KRLQIEAKVT VSACGALLTP 300 HLMLSSGLKN KNIGRNLHLH PVLMAWGYFP DLNLEFKGKN YEDGIITSVH KVVSADSKAK 360 AIIETPTLGL GTFSALCPWE FGEDIKNRML KFSRTVHLIS IIRDWGSRVV TKGGRDFFDM 420 VTADERPQSL VENWTTYSSA HQMRSCRMGI KAKEGVVDEN GES |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR02462 | pyranose_ox | 0.009 | 242 | 323 | 86 | + pyranose oxidase. Pyranose oxidase (also called glucose 2-oxidase) converts D-glucose and molecular oxygen to 2-dehydro-D-glucose and hydrogen peroxide. Peroxide production is believed to be important to the wood rot fungi in which this enzyme is found for lignin degradation. | ||
| pfam05199 | GMC_oxred_C | 0.0006 | 383 | 461 | 79 | + GMC oxidoreductase. This domain found associated with pfam00732. | ||
| pfam00732 | GMC_oxred_N | 5.0e-52 | 127 | 322 | 225 | + GMC oxidoreductase. This family of proteins bind FAD as a cofactor. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0009055 | electron carrier activity |
| GO:0016491 | oxidoreductase activity |
| GO:0016614 | oxidoreductase activity, acting on CH-OH group of donors |
| GO:0050660 | flavin adenine dinucleotide binding |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN71289.1 | 0 | 3 | 463 | 162 | 694 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002285334.1 | 0 | 3 | 463 | 162 | 694 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002311685.1 | 0 | 2 | 463 | 167 | 700 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002314488.1 | 0 | 3 | 463 | 140 | 672 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002528823.1 | 0 | 2 | 463 | 164 | 701 | disulfide oxidoreductase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4e0v_B | 0.001 | 27 | 108 | 7 | 76 | A Chain A, Structure Of L-Amino Acid Oxidase From The B. Jararacussu Venom |
| PDB | 4e0v_A | 0.001 | 27 | 108 | 7 | 76 | A Chain A, Structure Of L-Amino Acid Oxidase From The B. Jararacussu Venom |
| PDB | 3kve_D | 0.005 | 41 | 108 | 4 | 63 | A Chain A, Structure Of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization Of The Quaternary Structure By Divalent Ions And Structural Changes In The Dynamic Active Site |
| PDB | 3kve_C | 0.005 | 41 | 108 | 4 | 63 | A Chain A, Structure Of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization Of The Quaternary Structure By Divalent Ions And Structural Changes In The Dynamic Active Site |
| PDB | 3kve_B | 0.005 | 41 | 108 | 4 | 63 | A Chain A, Structure Of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization Of The Quaternary Structure By Divalent Ions And Structural Changes In The Dynamic Active Site |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO794753 | 540 | 2 | 463 | 0 |
| HO779224 | 401 | 50 | 425 | 0 |
| ES815664 | 255 | 161 | 415 | 0 |
| ES808761 | 255 | 172 | 426 | 0 |
| HO793330 | 240 | 156 | 392 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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